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eIF4E as a molecular wildcard in metazoans RNA metabolism

https://doi.org/10.1111/brv.13005
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inferredcites →https://doi.org/10.1002/1873-3468.12854openalex-snapshot
An in vivo proteomic analysis of the Me31B interactome in Drosophila germ granules
inferredcites →https://doi.org/10.1002/dvg.1020140603openalex-snapshot
Mechanism of action of developmentally regulated sea urchin inhibitor of eIF‐4
inferredcites →https://doi.org/10.1002/dvg.1020140604openalex-snapshot
Maturation hormone induced an increase in the translational activity of starfish oocytes coincident with the phosphorylation of the mRNA cap binding protein, eIF‐4E, and the activation of several kinases
inferredcites →https://doi.org/10.1002/pmic.200300555openalex-snapshot
Identification and characterization of the expression of the translation initiation factor 4A (eIF4A) from Drosophila melanogaster
inferredcites →https://doi.org/10.1002/wrna.52openalex-snapshot
Cap and cap‐binding proteins in the control of gene expression
inferredcites →https://doi.org/10.1006/dbio.2000.9943openalex-snapshot
Protein Kinase C-Related Kinase 2 Phosphorylates the Protein Synthesis Initiation Factor eIF4E in Starfish Oocytes
inferredcites →https://doi.org/10.1007/5584_2017_106openalex-snapshot
New Insights in Cardiac Calcium Handling and Excitation-Contraction Coupling
inferredcites →https://doi.org/10.1007/978-3-319-39468-8openalex-snapshot
Evolution of the Protein Synthesis Machinery and Its Regulation
inferredcites →https://doi.org/10.1007/978-3-319-39468-8_10openalex-snapshot
Evolution of eIF4E-Interacting Proteins
inferredcites →https://doi.org/10.1007/978-3-319-39468-8_15openalex-snapshot
Evolution of TOR and Translation Control
inferredcites →https://doi.org/10.1007/978-3-319-39468-8_19openalex-snapshot
Ribonucleoprotein Foci in Eukaryotes: How to Translate the Silence
inferredcites →https://doi.org/10.1007/978-3-319-39468-8_8openalex-snapshot
Expansion of eIF4E and 4E-BP Family Members in Deuterostomes
inferredcites →https://doi.org/10.1007/s00427-008-0268-2openalex-snapshot
Evolutionary origin and phylogenetic analysis of the novel oocyte-specific eukaryotic translation initiation factor 4E in Tetrapoda
inferredcites →https://doi.org/10.1007/s00436-019-06421-8openalex-snapshot
Functional characterization of the translation initiation factor eIF4E of Echinococcus granulosus
inferredcites →https://doi.org/10.1007/s004380050365openalex-snapshot
Localization, structure and expression of the gene for translation initiation factor eIF-4E from Drosophila melanogaster
inferredcites →https://doi.org/10.1007/s13238-017-0444-0openalex-snapshot
MicroRNAs recruit eIF4E2 to repress translation of target mRNAs
inferredcites →https://doi.org/10.1016/0014-5793(95)00081-jopenalex-snapshot
mRNA encoding the translation initiation factor eIF‐4E is expressed early in Xenopus embryogenesis
inferredcites →https://doi.org/10.1016/0167-4781(95)00039-jopenalex-snapshot
Translation initiation factor eIF-4E from Drosophila: cDNA sequence and expression of the gene
inferredcites →https://doi.org/10.1016/j.bbamcr.2012.03.013openalex-snapshot
Cap binding-independent recruitment of eIF4E to cytoplasmic foci
inferredcites →https://doi.org/10.1016/j.bbamcr.2021.119058openalex-snapshot
Connecting the “dots”: RNP granule network in health and disease
inferredcites →https://doi.org/10.1016/j.bbapap.2016.06.015openalex-snapshot
Diverse cap-binding properties of Drosophila eIF4E isoforms
inferredcites →https://doi.org/10.1016/j.bbcan.2020.188455openalex-snapshot
Translational control in the naked mole-rat as a model highly resistant to cancer
inferredcites →https://doi.org/10.1016/j.ceb.2009.01.027openalex-snapshot
Global implications of mRNA localization pathways in cellular organization
inferredcites →https://doi.org/10.1016/j.cell.2005.02.024openalex-snapshot
A New Paradigm for Translational Control: Inhibition via 5′-3′ mRNA Tethering by Bicoid and the eIF4E Cognate 4EHP
inferredcites →https://doi.org/10.1016/j.celrep.2015.04.065openalex-snapshot
The eIF4E-Binding Protein 4E-T Is a Component of the mRNA Decay Machinery that Bridges the 5′ and 3′ Termini of Target mRNAs
inferredcites →https://doi.org/10.1016/j.celrep.2016.01.036openalex-snapshot
Systemic Reprogramming of Translation Efficiencies on Oxygen Stimulus
inferredcites →https://doi.org/10.1016/j.celrep.2017.12.031openalex-snapshot
Oxygen-Sensitive Remodeling of Central Carbon Metabolism by Archaic eIF5B
inferredcites →https://doi.org/10.1016/j.celrep.2018.09.009openalex-snapshot
Maintenance of Proteostasis by P Body-Mediated Regulation of eIF4E Availability during Aging in Caenorhabditis elegans
inferredcites →https://doi.org/10.1016/j.celrep.2019.03.006openalex-snapshot
GIGYF1/2-Driven Cooperation between ZNF598 and TTP in Posttranscriptional Regulation of Inflammatory Signaling
inferredcites →https://doi.org/10.1016/j.celrep.2019.04.008openalex-snapshot
Nuclear eIF4E Stimulates 3′-End Cleavage of Target RNAs
inferredcites →https://doi.org/10.1016/j.celrep.2020.108262openalex-snapshot
4EHP and GIGYF1/2 Mediate Translation-Coupled Messenger RNA Decay
inferredcites →https://doi.org/10.1016/j.cub.2004.12.034openalex-snapshot
Diet-Dependent Effects of the Drosophila Mnk1/Mnk2 Homolog Lk6 on Growth via eIF4E
inferredcites →https://doi.org/10.1016/j.cub.2004.12.037openalex-snapshot
Drosophila Lk6 Kinase Controls Phosphorylation of Eukaryotic Translation Initiation Factor 4E and Promotes Normal Growth and Development
inferredcites →https://doi.org/10.1016/j.cub.2006.08.093openalex-snapshot
Cap-Dependent Translational Inhibition Establishes Two Opposing Morphogen Gradients in Drosophila Embryos
inferredcites →https://doi.org/10.1016/j.febslet.2012.05.059openalex-snapshot
4E‐BP3 regulates eIF4E‐mediated nuclear mRNA export and interacts with replication protein A2
inferredcites →https://doi.org/10.1016/j.jmb.2007.02.019openalex-snapshot
Structures of the Human eIF4E Homologous Protein, h4EHP, in its m7GTP-bound and Unliganded Forms
inferredcites →https://doi.org/10.1016/j.jmb.2007.06.033openalex-snapshot
Crystallographic and Mass Spectrometric Characterisation of eIF4E with N7-alkylated Cap Derivatives
inferredcites →https://doi.org/10.1016/j.jmb.2014.11.009openalex-snapshot
Distinct Features of Cap Binding by eIF4E1b Proteins
inferredcites →https://doi.org/10.1016/j.jmb.2023.167949openalex-snapshot
Drosophila Me31B is a Dual eIF4E-Interacting Protein
inferredcites →https://doi.org/10.1016/j.mod.2004.11.011openalex-snapshot
Functional analysis of seven genes encoding eight translation initiation factor 4E (eIF4E) isoforms in Drosophila
inferredcites →https://doi.org/10.1016/j.mod.2005.04.002openalex-snapshot
Functional diversity of the eukaryotic translation initiation factors belonging to eIF4 families
inferredcites →https://doi.org/10.1016/j.mod.2008.06.005openalex-snapshot
Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins
inferredcites →https://doi.org/10.1016/j.molbiopara.2010.11.011openalex-snapshot
The four trypanosomatid eIF4E homologues fall into two separate groups, with distinct features in primary sequence and biological properties
inferredcites →https://doi.org/10.1016/j.molbiopara.2020.111258openalex-snapshot
Translation initiation factors GleIF4E2 and GleIF4A can interact directly with the components of the pre-initiation complex to facilitate translation initiation in Giardia lamblia
inferredcites →https://doi.org/10.1016/j.tibs.2007.11.002openalex-snapshot
Was the initiation of translation in early eukaryotes IRES-driven?
inferredcites →https://doi.org/10.1016/j.tibs.2009.02.001openalex-snapshot
On the origin of the cap-dependent initiation of translation in eukaryotes
inferredcites →https://doi.org/10.1016/j.tibs.2009.10.009openalex-snapshot
Origins and evolution of the mechanisms regulating translation initiation in eukaryotes
inferredcites →https://doi.org/10.1016/j.tig.2022.04.003openalex-snapshot
The versatile relationships between eIF4E and eIF4E-interacting proteins
inferredcites →https://doi.org/10.1016/j.ydbio.2005.04.018openalex-snapshot
The expression profile of purified Drosophila germline stem cells
inferredcites →https://doi.org/10.1016/j.ydbio.2006.07.036openalex-snapshot
Translational control genes in the sea urchin genome
inferredcites →https://doi.org/10.1016/j.ydbio.2010.02.037openalex-snapshot
Different requirements for conserved post-transcriptional regulators in planarian regeneration and stem cell maintenance
inferredcites →https://doi.org/10.1016/j.ydbio.2015.12.021openalex-snapshot
Drosophila 4EHP is essential for the larval–pupal transition and required in the prothoracic gland for ecdysone biosynthesis
inferredcites →https://doi.org/10.1016/s0014-5793(02)03694-3openalex-snapshot
Localisation and regulation of the eIF4E‐binding protein 4E‐BP3
inferredcites →https://doi.org/10.1016/s0014-5793(97)00562-0openalex-snapshot
Disulfide bond formation is not involved in cap‐binding activity of Xenopus translation initiation factor eIF‐4E
inferredcites →https://doi.org/10.1016/s0021-9258(17)32415-8openalex-snapshot
Purification and characterization of eukaryotic polypeptide chain initiation factor 4F from Drosophila melanogaster embryos.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43324-8openalex-snapshot
Two forms of purified m7G-cap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells.
inferredcites →https://doi.org/10.1016/s0021-9258(18)99245-8openalex-snapshot
Multiple mRNAs encode the murine translation initiation factor eIF-4E
inferredcites →https://doi.org/10.1016/s0021-9258(19)49567-7openalex-snapshot
Changes in rates of protein synthesis and eukaryotic initiation factor-4 inhibitory activity in cell-free translation systems of sea urchin eggs and early cleavage stage embryos.
inferredcites →https://doi.org/10.1016/s0022-2836(02)00328-5openalex-snapshot
Biophysical Studies of eIF4E Cap-binding Protein: Recognition of mRNA 5′ Cap Structure and Synthetic Fragments of eIF4G and 4E-BP1 Proteins
inferredcites →https://doi.org/10.1016/s0092-8674(00)80280-9openalex-snapshot
Cocrystal Structure of the Messenger RNA 5′ Cap-Binding Protein (eIF4E) Bound to 7-methyl-GDP
inferredcites →https://doi.org/10.1016/s1534-5807(03)00400-3openalex-snapshot
Drosophila Cup Is an eIF4E Binding Protein that Associates with Bruno and Regulates oskar mRNA Translation in Oogenesis
inferredcites →https://doi.org/10.1021/bi00306a021openalex-snapshot
Functional characterization of eukaryotic mRNA cap binding protein complex: effects on translation of capped and naturally uncapped RNAs
inferredcites →https://doi.org/10.1021/bi0491651openalex-snapshot
Thermodynamics of mRNA 5‘ Cap Binding by Eukaryotic Translation Initiation Factor eIF4E
inferredcites →https://doi.org/10.1038/285331a0openalex-snapshot
Differential stimulation of capped mRNA translation in vitro by cap binding protein
inferredcites →https://doi.org/10.1038/35078571openalex-snapshot
The translational inhibitor 4E-BP is an effector of PI(3)K/Akt signalling and cell growth in Drosophila
inferredcites →https://doi.org/10.1038/cdd.2008.46openalex-snapshot
Depletion of the cap-associated isoform of translation factor eIF4G induces germline apoptosis in C. elegans
inferredcites →https://doi.org/10.1038/emboj.2009.53openalex-snapshot
Molecular dissection of the eukaryotic initiation factor 4E (eIF4E) export‐competent RNP
inferredcites →https://doi.org/10.1038/nature05603openalex-snapshot
eIF4E function in somatic cells modulates ageing in Caenorhabditis elegans
inferredcites →https://doi.org/10.1038/nature09715openalex-snapshot
The developmental transcriptome of Drosophila melanogaster
inferredcites →https://doi.org/10.1038/nature11055openalex-snapshot
An oxygen-regulated switch in the protein synthesis machinery
inferredcites →https://doi.org/10.1038/nature12962openalex-snapshot
Diversity and dynamics of the Drosophila transcriptome
inferredcites →https://doi.org/10.1038/ncomms11776openalex-snapshot
Translation control during prolonged mTORC1 inhibition mediated by 4E-BP3
inferredcites →https://doi.org/10.1038/ncomms6413openalex-snapshot
MNKs act as a regulatory switch for eIF4E1 and eIF4E3 driven mRNA translation in DLBCL
inferredcites →https://doi.org/10.1038/nrg3184openalex-snapshot
Translational control in cellular and developmental processes
inferredcites →https://doi.org/10.1038/nsb0997-717openalex-snapshot
Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein
inferredcites →https://doi.org/10.1038/onc.2017.372openalex-snapshot
Hypoxia activates cadherin-22 synthesis via eIF4E2 to drive cancer cell migration, invasion and adhesion
inferredcites →https://doi.org/10.1038/s41467-019-09086-0openalex-snapshot
A threonyl-tRNA synthetase-mediated translation initiation machinery
inferredcites →https://doi.org/10.1038/s41467-020-16504-1openalex-snapshot
A network of RNA-binding proteins controls translation efficiency to activate anaerobic metabolism
inferredcites →https://doi.org/10.1038/s41477-019-0553-2openalex-snapshot
A novel eIF4E-interacting protein that forms non-canonical translation initiation complexes
inferredcites →https://doi.org/10.1038/s41580-019-0118-2openalex-snapshot
Mechanisms and functions of ribosome-associated protein quality control
inferredcites →https://doi.org/10.1038/s41598-019-50357-zopenalex-snapshot
A ribosomal protein S5 isoform is essential for oogenesis and interacts with distinct RNAs in Drosophila melanogaster
inferredcites →https://doi.org/10.1038/s41598-020-57492-yopenalex-snapshot
Comparative Proteomics Reveal Me31B’s Interactome Dynamics, Expression Regulation, and Assembly Mechanism into Germ Granules during Drosophila Germline Development
inferredcites →https://doi.org/10.1038/sj.emboj.7600026openalex-snapshot
Drosophila Cup is an eIF4E‐binding protein that functions in Smaug‐mediated translational repression
inferredcites →https://doi.org/10.1038/sj.onc.1203473openalex-snapshot
The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA
inferredcites →https://doi.org/10.1042/bj20040769openalex-snapshot
The Drosophila protein kinase LK6 is regulated by ERK and phosphorylates the eukaryotic initiation factor eIF4E in vivo
inferredcites →https://doi.org/10.1042/bst0360671openalex-snapshot
Translational control in early development: CPEB, P-bodies and germinal granules
inferredcites →https://doi.org/10.1042/bst20140063openalex-snapshot
eIF4E-binding proteins: new factors, new locations, new roles
inferredcites →https://doi.org/10.1046/j.1432-0436.2000.066001015.xopenalex-snapshot
Alternative transcriptional initiation and splicing define the translational efficiencies of zebrafish mRNAs encoding eukaryotic initiation factor 4E
inferredcites →https://doi.org/10.1046/j.1432-0436.2002.700102.xopenalex-snapshot
The emerging roles of translation factor eIF4E in the nucleus
inferredcites →https://doi.org/10.1046/j.1432-1327.1998.2530027.xopenalex-snapshot
Isolation and characterization of the cDNA and the gene for eukaryotic translation initiation factor 4G from Drosophila melanogaster
inferredcites →https://doi.org/10.1073/pnas.0406451101openalex-snapshot
Cup is a nucleocytoplasmic shuttling protein that interacts with the eukaryotic translation initiation factor 4E to modulate Drosophila ovary development
inferredcites →https://doi.org/10.1073/pnas.0709128105openalex-snapshot
Drosophila germ-line modulation of insulin signaling and lifespan
inferredcites →https://doi.org/10.1073/pnas.100391597openalex-snapshot
Drosophila Thor participates in host immune defense and connects a translational regulator with innate immunity
inferredcites →https://doi.org/10.1073/pnas.1216862110openalex-snapshot
eIF4E3 acts as a tumor suppressor by utilizing an atypical mode of methyl-7-guanosine cap recognition
inferredcites →https://doi.org/10.1073/pnas.1524291113openalex-snapshot
Importin 8 mediates m 7 G cap-sensitive nuclear import of the eukaryotic translation initiation factor eIF4E
inferredcites →https://doi.org/10.1073/pnas.1701488114openalex-snapshot
Cap-binding protein 4EHP effects translation silencing by microRNAs
inferredcites →https://doi.org/10.1073/pnas.73.5.1559openalex-snapshot
A protein binding the methylated 5'-terminal sequence, m7GpppN, of eukaryotic messenger RNA.
inferredcites →https://doi.org/10.1073/pnas.75.10.4843openalex-snapshot
A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA.
inferredcites →https://doi.org/10.1073/pnas.76.9.4345openalex-snapshot
Eukaryotic mRNA cap binding protein: purification by affinity chromatography on sepharose-coupled m7GDP.
inferredcites →https://doi.org/10.1073/pnas.84.18.6359openalex-snapshot
Inhibitor of eukaryotic initiation factor 4F activity in unfertilized sea urchin eggs.
inferredcites →https://doi.org/10.1073/pnas.84.4.945openalex-snapshot
Amino acid sequence of the mRNA cap-binding protein from human tissues.
inferredcites →https://doi.org/10.1073/pnas.89.20.9612openalex-snapshot
A fraction of the mRNA 5' cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus.
inferredcites →https://doi.org/10.1073/pnas.93.3.1065openalex-snapshot
Translation initiation of ornithine decarboxylase and nucleocytoplasmic transport of cyclin D1 mRNA are increased in cells overexpressing eukaryotic initiation factor 4E.
inferredcites →https://doi.org/10.1074/jbc.270.36.21176openalex-snapshot
Eukaryotic Translation Initiation Factor 4E Regulates Expression of Cyclin D1 at Transcriptional and Post-transcriptional Levels
inferredcites →https://doi.org/10.1074/jbc.271.27.16393openalex-snapshot
Alternatively Spliced Transcripts from the Gene Produce Two Different Cap-binding Proteins
inferredcites →https://doi.org/10.1074/jbc.273.17.10325openalex-snapshot
Identification and Characterization of a Novel Cap-binding Protein from Arabidopsis thaliana
inferredcites →https://doi.org/10.1074/jbc.273.17.10538openalex-snapshot
Multiple Isoforms of Eukaryotic Protein Synthesis Initiation Factor 4E in Caenorhabditis elegans Can Distinguish between Mono- and Trimethylated mRNA Cap Structures
inferredcites →https://doi.org/10.1074/jbc.273.21.13104openalex-snapshot
Cloning and Characterization of 4EHP, a Novel Mammalian eIF4E-related Cap-binding Protein
inferredcites →https://doi.org/10.1074/jbc.275.14.10590openalex-snapshot
Functional Characterization of Five eIF4E Isoforms inCaenorhabditis elegans
inferredcites →https://doi.org/10.1074/jbc.m109.049858openalex-snapshot
Structural Insights into Parasite eIF4E Binding Specificity for m7G and m2,2,7G mRNA Caps
inferredcites →https://doi.org/10.1074/jbc.m113.471466openalex-snapshot
Hypoxia-inducible Factor-1α (HIF-1α) Promotes Cap-dependent Translation of Selective mRNAs through Up-regulating Initiation Factor eIF4E1 in Breast Cancer Cells under Hypoxia Conditions
inferredcites →https://doi.org/10.1074/jbc.m116.717363openalex-snapshot
Human Cells Cultured under Physiological Oxygen Utilize Two Cap-binding Proteins to recruit Distinct mRNAs for Translation
inferredcites →https://doi.org/10.1074/jbc.m313688200openalex-snapshot
Two Zebrafish eIF4E Family Members Are Differentially Expressed and Functionally Divergent
inferredcites →https://doi.org/10.1074/jbc.m407475200openalex-snapshot
Contribution of Trans-splicing, 5′ -Leader Length, Cap-Poly(A) Synergism, and Initiation Factors to Nematode Translation in an Ascaris suum Embryo Cell-free System
inferredcites →https://doi.org/10.1074/jbc.m704629200openalex-snapshot
CPEB Interacts with an Ovary-specific eIF4E and 4E-T in Early Xenopus Oocytes
inferredcites →https://doi.org/10.1080/21690731.2016.1220899openalex-snapshot
The eukaryotic translation initiation factor eIF4E wears a “cap” for many occasions
inferredcites →https://doi.org/10.1083/jcb.148.2.239openalex-snapshot
Nuclear Eukaryotic Initiation Factor 4e (Eif4e) Colocalizes with Splicing Factors in Speckles
inferredcites →https://doi.org/10.1083/jcb.150.2.f51openalex-snapshot
The Drosophila melanogaster Genome
inferredcites →https://doi.org/10.1083/jcb.200309088openalex-snapshot
Cup is an eIF4E binding protein required for both the translational repression of oskar and the recruitment of Barentsz
inferredcites →https://doi.org/10.1083/jcb.200501019openalex-snapshot
eIF4E promotes nuclear export of cyclin D1 mRNAs via an element in the 3′UTR
inferredcites →https://doi.org/10.1083/jcb.200504039openalex-snapshot
A role for the eIF4E-binding protein 4E-T in P-body formation and mRNA decay
inferredcites →https://doi.org/10.1083/jcb.200607020openalex-snapshot
eIF4E is a central node of an RNA regulon that governs cellular proliferation
inferredcites →https://doi.org/10.1083/jcb.200903003openalex-snapshot
An eIF4E-binding protein regulates katanin protein levels in C. elegans embryos
inferredcites →https://doi.org/10.1093/emboj/19.12.3142openalex-snapshot
A novel shuttling protein, 4E‐T, mediates the nuclear import of the mRNA 5′ cap‐binding protein, eIF4E
inferredcites →https://doi.org/10.1093/emboj/20.16.4547openalex-snapshot
PML RING suppresses oncogenic transformation by reducing the affinity of eIF4E for mRNA
inferredcites →https://doi.org/10.1093/emboj/cdf473openalex-snapshot
Discrimination between mono–and trimethylated cap structures by two isoforms of Caenorhabditis elegans eIF4E
inferredcites →https://doi.org/10.1093/emboj/cdg069openalex-snapshot
The proline‐rich homeodomain protein, PRH, is a tissue‐specific inhibitor of eIF4E‐dependent cyclin D1 mRNA transport and growth
inferredcites →https://doi.org/10.1093/genetics/iyab195openalex-snapshot
Germ granules and gene regulation in the Caenorhabditis elegans germline
inferredcites →https://doi.org/10.1093/nar/gkab971openalex-snapshot
FlyAtlas 2 in 2022: enhancements to the Drosophila melanogaster expression atlas
inferredcites →https://doi.org/10.1093/nar/gkh303openalex-snapshot
The active form of Xp54 RNA helicase in translational repression is an RNA-mediated oligomer
inferredcites →https://doi.org/10.1093/nar/gkr650openalex-snapshot
Structural basis for nematode eIF4E binding an m 2,2,7 G-Cap and its implications for translation initiation
inferredcites →https://doi.org/10.1093/nar/gkv564openalex-snapshot
The eIF3 complex ofLeishmania—subunit composition and mode of recruitment to different cap-binding complexes
inferredcites →https://doi.org/10.1093/nar/gkz429openalex-snapshot
Direct role for the Drosophila GIGYF protein in 4EHP-mediated mRNA repression
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a022532openalex-snapshot
Binding Analysis of Xenopus laevis Translation Initiation Factor 4E (eIF4E) in Initiation Complex Formation
inferredcites →https://doi.org/10.1101/cshperspect.a032607openalex-snapshot
Principles of Translational Control
inferredcites →https://doi.org/10.1101/cshperspect.a032813openalex-snapshot
Stress Granules and Processing Bodies in Translational Control
inferredcites →https://doi.org/10.1101/cshperspect.a033050openalex-snapshot
Phosphorylation and Signal Transduction Pathways in Translational Control
inferredcites →https://doi.org/10.1101/gad.13.20.2704openalex-snapshot
Recruitment of Nanos to hunchback mRNA by Pumilio
inferredcites →https://doi.org/10.1101/gad.1471006openalex-snapshot
Cracking the egg: molecular dynamics and evolutionary aspects of the transition from the fully grown oocyte to embryo
inferredcites →https://doi.org/10.1101/gad.299420.117openalex-snapshot
GIGYF1/2 proteins use auxiliary sequences to selectively bind to 4EHP and repress target mRNA expression
inferredcites →https://doi.org/10.1101/gad.336073.119openalex-snapshot
4E-T-bound mRNAs are stored in a silenced and deadenylated form
inferredcites →https://doi.org/10.1101/gad.870801openalex-snapshot
Drosophila Brain Tumor is a translational repressor
inferredcites →https://doi.org/10.1101/gr.10.8.1172openalex-snapshot
Eukaryote-specific Domains in Translation Initiation Factors: Implications for Translation Regulation and Evolution of the Translation System
inferredcites →https://doi.org/10.1101/gr.202150.115openalex-snapshot
Trans-splicing enhances translational efficiency in C. elegans
inferredcites →https://doi.org/10.1111/febs.16275openalex-snapshot
eIF4E‐homologous protein (4EHP): a multifarious cap‐binding protein
inferredcites →https://doi.org/10.1111/imr.12240openalex-snapshot
The eukaryotic translation initiation factor eIF 4E in the nucleus: taking the road less traveled
inferredcites →https://doi.org/10.1111/j.1432-1033.2004.04149.xopenalex-snapshot
Characterization of mammalian eIF4E‐family members
inferredcites →https://doi.org/10.1111/j.1753-4887.1981.tb06752.xopenalex-snapshot
Proceedings of the National Academy of Sciences of the United States of America
inferredcites →https://doi.org/10.1126/science.860134openalex-snapshot
Evolution and Tinkering
inferredcites →https://doi.org/10.1128/mcb.00070-18openalex-snapshot
Signaling Pathways Involved in the Regulation of mRNA Translation
inferredcites →https://doi.org/10.1128/mcb.00128-07openalex-snapshot
P-Body Formation Is a Consequence, Not the Cause, of RNA-Mediated Gene Silencing
inferredcites →https://doi.org/10.1128/mcb.00455-12openalex-snapshot
A Novel 4EHP-GIGYF2 Translational Repressor Complex Is Essential for Mammalian Development
inferredcites →https://doi.org/10.1128/mcb.00845-15openalex-snapshot
Tristetraprolin Recruits Eukaryotic Initiation Factor 4E2 To Repress Translation of AU-Rich Element-Containing mRNAs
inferredcites →https://doi.org/10.1128/mcb.01354-12openalex-snapshot
Mextli Is a Novel Eukaryotic Translation Initiation Factor 4E-Binding Protein That Promotes Translation in Drosophila melanogaster
inferredcites →https://doi.org/10.1128/mcb.22.6.1656-1663.2002openalex-snapshot
Phosphorylation of Eukaryotic Translation Initiation Factor 4E Is Critical for Growth
inferredcites →https://doi.org/10.1128/mcb.23.24.9117-9126.2003openalex-snapshot
Signaling from Akt to FRAP/TOR Targets both 4E-BP and S6K in Drosophila melanogaster
inferredcites →https://doi.org/10.1128/mcb.25.1.100-113.2005openalex-snapshot
Translation of a Small Subset of Caenorhabditis elegans mRNAs Is Dependent on a Specific Eukaryotic Translation Initiation Factor 4E Isoform
inferredcites →https://doi.org/10.1128/mcb.25.3.1100-1112.2005openalex-snapshot
Eukaryotic Translation Initiation Factor 4E Activity Is Modulated by HOXA9 at Multiple Levels
inferredcites →https://doi.org/10.1128/mcb.9.5.2181openalex-snapshot
Purification and characterization of mRNA cap-binding protein from Drosophila melanogaster embryos.
inferredcites →https://doi.org/10.1146/annurev-biochem-013118-111042openalex-snapshot
The Organizing Principles of Eukaryotic Ribosome Recruitment
inferredcites →https://doi.org/10.1146/annurev-biochem-060713-035802openalex-snapshot
The Scanning Mechanism of Eukaryotic Translation Initiation
inferredcites →https://doi.org/10.1155/2012/134839openalex-snapshot
Diversity of Eukaryotic Translational Initiation Factor eIF4E in Protists
inferredcites →https://doi.org/10.1155/2012/287852openalex-snapshot
Conservation of the RNA Transport Machineries and Their Coupling to Translation Control across Eukaryotes
inferredcites →https://doi.org/10.1155/2012/960420openalex-snapshot
The Distribution of eIF4E-Family Members across Insecta
inferredcites →https://doi.org/10.1158/0008-5472.can-13-2278openalex-snapshot
Cancer Cells Exploit eIF4E2-Directed Synthesis of Hypoxia Response Proteins to Drive Tumor Progression
inferredcites →https://doi.org/10.1182/blood-2015-05-645069openalex-snapshot
Combinatorial targeting of nuclear export and translation of RNA inhibits aggressive B-cell lymphomas
inferredcites →https://doi.org/10.1186/1471-2148-5-48openalex-snapshot
Phylogenetic analysis of eIF4E-family members
inferredcites →https://doi.org/10.1186/gb-2010-11-s1-i11openalex-snapshot
The developmental transcriptome of Drosophila melanogaster
inferredcites →https://doi.org/10.1186/s12862-015-0301-9openalex-snapshot
The alveolate translation initiation factor 4E family reveals a custom toolkit for translational control in core dinoflagellates
inferredcites →https://doi.org/10.1186/s12867-016-0072-xopenalex-snapshot
Distinct recruitment of human eIF4E isoforms to processing bodies and stress granules
inferredcites →https://doi.org/10.1242/bio.011585openalex-snapshot
The canonical eIF4E isoform ofC. elegansregulates growth, embryogenesis, and germline sex-determination
inferredcites →https://doi.org/10.1242/dev.003517openalex-snapshot
A novel eIF4G homolog, Off-schedule, couples translational control to meiosis and differentiation inDrosophilaspermatocytes
inferredcites →https://doi.org/10.1242/dev.003764openalex-snapshot
Translational control of meiotic cell cycle progression and spermatid differentiation in male germ cells by a novel eIF4G homolog
inferredcites →https://doi.org/10.1242/dev.02276openalex-snapshot
Degrade to create: developmental requirements for ubiquitin-mediated proteolysis during earlyC. elegansembryogenesis
inferredcites →https://doi.org/10.1242/dev.055327openalex-snapshot
zif-1translational repression defines a second, mutually exclusive OMA function in germline transcriptional repression
inferredcites →https://doi.org/10.1242/dev.073122openalex-snapshot
Eukaryotic initiation factor 4E-3 is essential for meiotic chromosome segregation, cytokinesis and male fertility in Drosophila
inferredcites →https://doi.org/10.1242/dev.128.20.3899openalex-snapshot
An isoform of eIF4E is a component of germ granules and is required for spermatogenesis inC. elegans
inferredcites →https://doi.org/10.1242/dev.183053openalex-snapshot
Drosophila doublefault protein coordinates multiple events during male meiosis by controlling mRNA translation
inferredcites →https://doi.org/10.1242/dev.200477openalex-snapshot
Eukaryotic translation initiation factor eIF4E-5 is required for spermiogenesis in Drosophila melanogaster
inferredcites →https://doi.org/10.1242/jcs.03339openalex-snapshot
After fertilization of sea urchin eggs, eIF4G is post-translationally modified and associated with the cap-binding protein eIF4E
inferredcites →https://doi.org/10.1242/jcs.046771openalex-snapshot
A germline-specific isoform of eIF4E (IFE-1) is required for efficient translation of stored mRNAs and maturation of both oocytes and sperm
inferredcites →https://doi.org/10.1242/jcs.063107openalex-snapshot
AC. eleganseIF4E-family member upregulates translation at elevated temperatures of mRNAs encoding MSH-5 and other meiotic crossover proteins
inferredcites →https://doi.org/10.1242/jcs.119834openalex-snapshot
ifet-1 is a broad scale translational repressor required for normal P granule formation in C. elegans
inferredcites →https://doi.org/10.1242/jcs.172684openalex-snapshot
Spatial and temporal translational control of germ cell mRNAs mediated by the eIF4E isoform IFE-1
inferredcites →https://doi.org/10.1242/jcs.237990openalex-snapshot
Distinct roles of two eIF4E isoforms in the germline of Caenorhabditis elegans
inferredcites →https://doi.org/10.1242/jcs.258757openalex-snapshot
me31B regulates stem cell homeostasis by preventing excess dedifferentiation in the Drosophila male germline
inferredcites →https://doi.org/10.1261/rna.045534.114openalex-snapshot
eIF4F-like complexes formed by cap-binding homolog TbEIF4E5 with TbEIF4G1 or TbEIF4G2 are implicated in post-transcriptional regulation in Trypanosoma brucei
inferredcites →https://doi.org/10.1261/rna.060137.116openalex-snapshot
A biochemical framework for eIF4E-dependent mRNA export and nuclear recycling of the export machinery
inferredcites →https://doi.org/10.1261/rna.2340405openalex-snapshot
A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
inferredcites →https://doi.org/10.1261/rna.453107openalex-snapshot
Weak binding affinity of human 4EHP for mRNA cap analogs
inferredcites →https://doi.org/10.1261/rna.7154104openalex-snapshot
Internal ribosome entry site drives cap-independent translation of reaper and heat shock protein 70 mRNAs in Drosophila embryos
inferredcites →https://doi.org/10.1261/rna.950608openalex-snapshot
Control of eIF4E cellular localization by eIF4E-binding proteins, 4E-BPs
inferredcites →https://doi.org/10.1271/bbb.65.229openalex-snapshot
Translational Regulation of the mRNA Encoding the Eukaryotic Translation Initiation Factor 4E in Xenopus
inferredcites →https://doi.org/10.1271/bbb.65.232openalex-snapshot
Analysis of the Isoform of Xenopus Euakryotic Translation Initiation Factor 4E
inferredcites →https://doi.org/10.1371/journal.pgen.1002185openalex-snapshot
The Translation Initiation Factor eIF4E Regulates the Sex-Specific Expression of the Master Switch Gene Sxl in Drosophila melanogaster
inferredcites →https://doi.org/10.1371/journal.pone.0072761openalex-snapshot
Investigating the Consequences of eIF4E2 (4EHP) Interaction with 4E-Transporter on Its Cellular Distribution in HeLa Cells
inferredcites →https://doi.org/10.1371/journal.pone.0122519openalex-snapshot
Loss-of-Function Analysis Reveals Distinct Requirements of the Translation Initiation Factors eIF4E, eIF4E-3, eIF4G and eIF4G2 in Drosophila Spermatogenesis
inferredcites →https://doi.org/10.1371/journal.pone.0267156openalex-snapshot
Interplay between SERCA, 4E-BP, and eIF4E in the Drosophila heart
inferredcites →https://doi.org/10.1530/rep-09-0083openalex-snapshot
Molecular mechanisms of gene regulation during Drosophila spermatogenesis
inferredcites →https://doi.org/10.1534/genetics.107.083097openalex-snapshot
Regulation of Neurogenesis and Epidermal Growth Factor Receptor Signaling by the Insulin Receptor/Target of Rapamycin Pathway in Drosophila
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Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4883561openalex-extracted
Screening of Transcription Factor Families of Galeruca Daurica (Joannis) in Response to Low Temperature Stress Based on Transcriptome Analysis
inferred← citeshttps://doi.org/10.1016/j.jbc.2024.108129openalex-snapshot
Analysis of eIF4E-family members in fungi contributes to their classification in eukaryotes
inferred← citeshttps://doi.org/10.1042/bcj20253170openalex-snapshot
RNMT-dependent RNA cap methylation in health and disease
inferred← citeshttps://doi.org/10.1080/19491034.2024.2360196openalex-snapshot
eIF4E orchestrates mRNA processing, RNA export and translation to modify specific protein production
inferred← citeshttps://doi.org/10.1101/2024.02.20.581179openalex-snapshot
Regulated mRNA recruitment in dinoflagellates is reflected in hyper-variable mRNA spliced leaders and novel eIF4Es
inferred← citeshttps://doi.org/10.1111/febs.70521openalex-snapshot
Maternal redd1 mRNA decline triggers mTORC1 activation during the blastula–gastrula transition in zebrafish embryos
inferred← citeshttps://doi.org/10.20517/and.2024.15openalex-snapshot
Circadian rhythm in neurodegenerative disease: the role of RNA modifications and potential application of RNA-based therapeutics
inferred← citeshttps://doi.org/10.3390/ijms25147834openalex-snapshot
Functional Characterization of Six Eukaryotic Translation Initiation Factors of Toxoplasma gondii Using the CRISPR-Cas9 System
inferred← citeshttps://doi.org/10.3390/ijms26188758openalex-snapshot
Deep Sequencing Reveals Novel Mutations in Androgen Receptor-Related Genes in Prostate Cancer
inferred← citeshttps://doi.org/10.3390/ijms27156911openalex-snapshot
Med9 Is a Novel eIF4E-Interacting Protein in Saccharomyces cerevisiae
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